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Literature summary extracted from

  • Gouda, M.D.; Singh, S.A.; Rao, A.G.; Thakur, M.S.; Karanth, N.G.
    Thermal inactivation of glucose oxidase. Mechanism and stabilization using additives (2003), J. Biol. Chem., 278, 24324-24333.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.1.3.4 K2SO4 enhances the thermal stability by primarily strengthening the hydrophobic interactions and makes the holoenzyme a more compact dimeric structure Aspergillus niger
1.1.3.4 the stabilization of the enzyme by NaCl and lysozyme is primarily the result of charge neutralization Aspergillus niger

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.3.4 160000
-
gel filtration Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.4 Aspergillus niger
-
type VII-S
-

Subunits

EC Number Subunits Comment Organism
1.1.3.4 dimer
-
Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.3.4 additional information
-
the irreversible nature of thermal inactivation is caused by a change in the state of association of apoenzyme. The dissociation of FAD results in the loss of secondary and tertiary structure, leading the unfolding and nonspecific aggregation of the enzyme molecule because of hydrophobic interactions of side chains Aspergillus niger
1.1.3.4 56
-
half-life of native enzyme without additive: 86 min, half-life of enzyme in presence of lysozyme: 322 min, half-life of enzyme in presence of 1 M NaCl: 1806 min, half-life of enzyme in presence of 0.2 M K2SO4: 1446 min Aspergillus niger
1.1.3.4 59
-
midpoint for thermal inactivation of residual activity and dissocation of FAD Aspergillus niger
1.1.3.4 60
-
half-life of native enzyme without additive: 13 min, half-life of enzyme in presence of lysozyme: 46 min, half-life of enzyme in presence of 1 M NaCl: 434 min, half-life of enzyme in presence of 0.2 M K2SO4: 308 min Aspergillus niger
1.1.3.4 62
-
midpoint for loss of secondary and tertiary structure Aspergillus niger
1.1.3.4 63
-
half-life of native enzyme without additive: 7.5 min, half-life of enzyme in presence of lysozyme: 24 min, half-life of enzyme in presence of 1 M NaCl: 146 min, half-life of enzyme in presence of 0.2 M K2SO4: 62 min Aspergillus niger
1.1.3.4 67
-
half-life of native enzyme without additive: 4.5 min, half-life of enzyme in presence of lysozyme: 12 min, half-life of enzyme in presence of 1 M NaCl: 58 min, half-life of enzyme in presence of 0.2 M K2SO4: 27.5 min Aspergillus niger

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.4 FAD dissociation of FAD from the holoenzyme is responsible for the thermal inaction of the enzyme Aspergillus niger